Sulfhydryl groups are involved in H+ translocation via the uncoupling protein of brown adipose tissue mitochondria

FEBS Letters

Ježek, Petr¹ 

[1] Institute of Physiology, Czechoslovak Academy of Sciences, Videňska 1083, CS-142 20 Prague 4, Czechoslovakia

关键词: Mersalyl;    Uncoupling protein;    Sulfhydryl reagent;    H+ transport;    Sulfhydryl group;    (Brown-fat mitochondria);    BAT;    brown adipose tissue;    BSA;    bovine serum albumin;    CCCP;    carbonyl cyanide m-chlorophenylhydrazone;    DCCD;    dicyclohexylcar-bodiimide;    DTNB;    5;    5'-dithiobis(2-nitrobenzoate);    EMA;    eosin-5-maleimide;    NEM;    N-efhylmaleimide;    PMB;    p-hydroxymercuribenzoate;    TBT;    tributyltin chloride;    UP;    uncoupling protein;   

DOI  :  10.1016/0014-5793(87)81280-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mersalyl inhibits H⁺ transport via the uncoupling protein (UP) in brown adipose tissue (BAT) mitochondria estimated as swelling in potassium acetate (K _i 67 μM) or as valinomycin-induced H⁺ extrusion in K ₂SO₄ (K _i 55 μM) and KCl. The swelling in KCl is depressed only slightly. Some other SH-reagents (p-hydroxymercuribenzoate, 5,5'-dithiobis(2-nitrobenzoate) and thiolyte DB), but not hydrophobic reagents (N-ethylmaleimide and eosin-5-maleimide), exhibit analogous inhibition. Thus an essential SH-group localized at the water-accessible cytosolic surface of UP was found to be involved in H⁺ transport via UP but not in Cl⁻ transport.

【 授权许可】

Unknown